A human poly(ADP-ribose) polymerase gene family (ADPRTL): cDNA cloning of two novel poly(ADP-ribose) polymerase homologues

Genomics. 1999 May 1;57(3):442-5. doi: 10.1006/geno.1999.5799.


Posttranscriptional modification of nuclear proteins by poly(ADP-ribosyl)ation in response to DNA strand breaks plays an important role in DNA repair, regulation of apoptosis, and maintenance of genomic stability. A 113-kDa human poly(ADP-ribose) polymerase (PARP) has previously been identified and cloned. However, there is evidence that additional enzymes with PARP activity exist in mammalian cells. I have identified and cloned the cDNAs of two novel approximately 60-kDa human proteins that are 40 and 31% identical to the catalytic C-terminal domain of PARP. These proteins, named PARP-2 and PARP-3, lack the DNA-binding and automodification domains. PARP-2 and PARP-3 mRNAs were detected in 16 different human tissues as major bands of 2.0 and 2.2 kb, respectively. Radiation hybrid analysis assigned the PARP-2 gene (HGMW-approved symbol ADPRTL2) to chromosome 14q11.2-q12 and the PARP-3 gene (HGMW-approved symbol ADPRTL3) to 3p21.1-p22.2. This report shows the existence of a human PARP gene family with at least three closely related members.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Cloning, Molecular
  • DNA, Complementary
  • Humans
  • Molecular Sequence Data
  • Poly(ADP-ribose) Polymerases / genetics*


  • DNA, Complementary
  • Poly(ADP-ribose) Polymerases

Associated data

  • GENBANK/AF083068
  • GENBANK/AF085734